Structure of limonene synthase, a simple model for terpenoid cyclase catalysis
Structure of limonene synthase, a simple model for terpenoid cyclase catalysis
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DOI：
10.1073/pnas.0700915104
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发表时间：
2007-03-27
影响因子：
11.1
通讯作者：
Kang, Chulhee
中科院分区：
文献类型：
--
作者：
Hyatt, David C.;Youn, Buhyun;Kang, Chulhee
Meniha spicata的(4S)-柠檬烯合成酶是一种金属离子依赖的单萜环化酶，催化香叶基二磷酸的偶联异构化和环化反应，其晶体结构以2.7埃分辨率被分别连接到底物和中间体的两种形式--2-氟三羟基二磷酸和2-氟丙酰-二磷酸。这些发现对同源二聚体中的结构域相互作用以及在多步反应过程中二磷酸-金属离子配位和底物结合构象的变化的影响进行了描述。
The crystal structure of (4S)-limonene synthase from Meniha spicata, a metal ion-dependent monoterpene cyclase that catalyzes the coupled isomerization and cyclization of geranyl diphosphate, is reported at 2.7-angstrom resolution in two forms liganded to the substrate and intermediate analogs, 2-fluorogeranyl diphosphate and 2-fluorolinalyl diphosphate, respectively. The implications of these findings are described for domain interactions in the homodimer and for changes in diphosphate-metal ion coordination and substrate binding conformation in the course of the multistep reaction.